Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/6565
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dc.contributor.authorKolaj-Robin, Olgaen
dc.contributor.authorSoulimane, Tewfik-
dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorKoutsoupakis, Constantinos-
dc.contributor.otherΒαρώτσης, Κωνσταντίνος-
dc.contributor.otherΚουτσουπάκης, Κωνσταντίνος-
dc.date.accessioned2013-01-17T08:23:57Zen
dc.date.accessioned2013-05-17T07:13:10Z-
dc.date.accessioned2015-12-08T07:53:50Z-
dc.date.available2013-01-17T08:23:57Zen
dc.date.available2013-05-17T07:13:10Z-
dc.date.available2015-12-08T07:53:50Z-
dc.date.issued2011en
dc.identifier.citationJournal of biological chemistry, 2011, Volume 286, Issue 35, Pages 30600-30605en
dc.identifier.issn00219258en
dc.identifier.urihttp://ktisis.cut.ac.cy/handle/10488/6565en
dc.description.abstractElucidating the properties of the heme Fe-Cu B binuclear center and the dynamics of the protein response in cytochrome c oxidase is crucial to understanding not only the dioxygen activation and bond cleavage by the enzyme but also the events related to the release of the produced water molecules. The time-resolved step-scan FTIR difference spectra show the ν 7a(CO) of the protonated form of Tyr residues at 1247 cm -1 and that of the deprotonated form at 1301 cm -1. By monitoring the intensity changes of the 1247 and 1301 cm -1 modes as a function of pH, we measured a pK a of 7.8 for the observed tyrosine. The FTIR spectral changes associated with the tyrosine do not belong to Tyr-237 but are attributed to the highly conserved in heme-copper oxidases Tyr-136 and/or Tyr-133 residue (Koutsoupakis, K., Stavrakis, S., Pinakoulaki, E., Soulimane, T., and Varotsis, C. (2002) J. Biol. Chem. 277, 32860-32866). The oxygenation of CO by the mixed-valence form of the enzyme revealed the formation of the ∼607 nm P (Fe(IV)=O) species in the pH 6-9 range and the return to the oxidized form without the formation of the 580 nm F form. The data indicate that Tyr-237 is not involved in the proton transfer pathway in the oxygenation of CO by the mixed-valence form of the enzyme. The implication of these results with respect to the role of Tyr-136 and Tyr-133 in proton transfer/gating along with heme a 3 ringD propionate-H 2O-ring A propionate-Asp-372 site to the exit/output proton channel (H 2O pool) is discusseden
dc.formatpdfen
dc.language.isoenen
dc.publisherThe American Society for Biochemistry and Molecular Biologyen
dc.rights© 2011 by The American Society for Biochemistry and Molecular Biology, Incen
dc.subjectAmino acidsen
dc.subjectEnzymesen
dc.subjectLakesen
dc.subjectFourier transform infrared spectroscopyen
dc.subjectOxygenatorsen
dc.subjectPorphyrinsen
dc.subjectProtonsen
dc.subjectSpectroscopyen
dc.subjectTyrosineen
dc.titleProbing protonation/deprotonation of tyrosine residues in cytochrome ba 3 oxidase from thermus thermophilus by time-resolved step-scan fourier transform infrared spectroscopyen
dc.typeArticleen
dc.collaborationCyprus University of Technology-
dc.collaborationUniversity of Limerick-
dc.subject.categoryPhysical Sciences-
dc.journalsSubscription-
dc.reviewPeer Reviewed-
dc.countryCyprus-
dc.countryIreland-
dc.subject.fieldNatural Sciences-
dc.identifier.doi10.1074/jbc.M111.252213en
dc.identifier.pmid21757723-
dc.dept.handle123456789/77en
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_6501-
item.openairetypearticle-
item.grantfulltextnone-
item.languageiso639-1en-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.orcid0000-0001-9301-1021-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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